Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Fibrinopeptide A release is necessary for effective B:b interactions in polymerisation of variant fibrinogens with impaired A:a interactions.

Thrombosis and haemostasis - 1 Feb 2013

Soya Keisuke, Terasawa Fumiko, Okumura Nobuo

Abstract excerpt

Fibrin polymerisation is mediated by interactions between knobs 'A' and 'B' exposed by thrombin cleavage, and holes 'a' and 'b'. We demonstrated markedly delayed thrombin-catalysed fibrin polymerisation, through B:b interactions alone, of recombinant γD364H -fibrinogen with impaired hole 'a'. To determine whether recombinant variant fibrinogens with no release of fibrinopeptide A (FpA) polymerise similarly to...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Catalysis
Share to Fibrin
Share to Fibrinogen

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Fibrinogens, Abnormal

Share to Fibrinolytic Agents

Share to Microscopy, Electron, Scanning

Share to Polymerization

Share to Thrombin

Source

Identifiers

PMID: 23238100
DOI: 10.1160/TH12-09-0684

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Fibrinopeptide A release is necessary for effective B:b interactions in polymerisation of variant fibrinogens with impaired A:a interactions.PMID 23238100Read ↗

B:b interactions are essential for polymerization of variant fibrinogens with impaired holes 'a'.Semantic proximity Read ↗

Homophenotypic Aalpha R16H fibrinogen (Kingsport): uniquely altered polymerization associated with slower fibrinopeptide A than fibrinopeptide B release.Semantic proximity Read ↗

Fibrinogen Magdeburg I: a novel variant of human fibrinogen with an amino acid exchange in the fibrinopeptide A (Aalpha 9, Leu-->Pro).Semantic proximity Read ↗

Incorporation of fibrin molecules containing fibrinopeptide A alters clot ultrastructure and decreases permeability.Semantic proximity Read ↗

An engineered fibrinogen variant AαQ328,366P does not polymerise normally, but retains the ability to form α cross-links.Semantic proximity Read ↗

Decreased lateral aggregation of a variant recombinant fibrinogen provides insight into the polymerization mechanism.Semantic proximity Read ↗

Exon skipping and aberrant signal peptide cleavage produce novel fibrinogen with an Aα chain lacking the first 42 residues.Semantic proximity Read ↗

Partial deletion of the αC-domain in the Fibrinogen Perth variant is associated with thrombosis, increased clot strength and delayed fibrinolysis.Semantic proximity Read ↗

Analysis of engineered fibrinogen variants suggests that an additional site mediates platelet aggregation and that "B-b" interactions have a role in protofibril formation.Semantic proximity Read ↗

Fibrinogen residue γAla341 is necessary for calcium binding and 'A-a' interactions.Semantic proximity Read ↗

Fibrinogen Matsumoto V: a variant with Aalpha19 Arg-->Gly (AGG-->GGG). Comparison between fibrin polymerization stimulated by thrombin or reptilase and fibrin monomer polymerization.Semantic proximity Read ↗

Substoichiometric molecular control and amplification of the initiation and nature of amyloid fibril formation: lessons from and for blood clottingSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.